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- W2954658896 abstract "Cell BiologyMultiple innate immune sensors undergo rapid assembly into large complexes known as signalosomes. This is an essential step during cellular responses to microbes and danger signals. How this process is regulated to avoid accumulation of potentially toxic protein aggregates remains poorly understood. Abdel-Nour et al. identified a pathway, dependent on heme-regulated inhibitor, eukaryotic initiation factor 2α, activating transcription factor 4, and heat shock protein B8, which controls the folding and scaffolding of innate immune sensors, allowing optimal proinflammatory signaling (see the Perspective by Pierre). The pathway appears to mirror the endoplasmic reticulum unfolded protein response (UPR), and so was named the cytosolic UPR (cUPR). The cUPR may represent a general mechanism to control protein misfolding in cells.Science , this issue p. [eaaw4144][1]; see also p. [28][2] [1]: /lookup/doi/10.1126/science.aaw4144 [2]: /lookup/doi/10.1126/science.aay0987" @default.
- W2954658896 created "2019-07-12" @default.
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- W2954658896 date "2019-07-04" @default.
- W2954658896 modified "2023-09-25" @default.
- W2954658896 title "Linking protein misfolding and innate immunity" @default.
- W2954658896 doi "https://doi.org/10.1126/science.365.6448.40-n" @default.
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